YARS (1-528, His-Tag) Human Protein
Specifications
| Product Data | |
| Species | Human |
|---|---|
| Expression Host | E. coli |
| Expression cDNA Clone or AA Sequence | |
| Tag | His-Tag |
| Predicted MW | 61.3 kDa (548aa) |
| Concentration | 1mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Presentation State | Purified |
| Buffer | Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol, 0.1M NaCl |
| Preparation | Liquid purified protein |
| Recommended Dilution | SDS-PAGE |
| Protein Description | Recombinant human YARS protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Storage | Can be stored at +2°C to +8°C for 1 week. For long term storage, aliquot and store at -20°C to -80C. Avoid repeated freezing and thawing cycles. |
| Stability | Shelf life: one year from despatch. |
| Shipping | Blue Ice |
| Reference Data | |
| RefSeq | NP_003671.1 |
| Locus ID | 8565 |
| UniProt ID | P54577 |
| Cytogenetics | 1p35.1 |
| Synonyms | Tyrosyl-tRNA synthetase, CMTDIC, TYRRS, YRS, YTS |
| Summary | Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine. provided by RefSeq, Jul 2008 |
| Protein Categories | Cytokines, Enzyme: Ligase, Intracellular Proteins, Nervous system: Neurodegenerative diseases |
| Protein Families | Druggable Genome |
| Protein Pathways | Aminoacyl-tRNA biosynthesis |
Reviews
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Resources
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Citations
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